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Literature summary for 3.1.3.1 extracted from

  • Tibbitts, T.T.; Xu, X.; Kantrowitz, E.R.
    Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp-369->Asn): a mechanism involving one zinc per active site (1994), Protein Sci., 3, 2005-2014.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D369A mutant enzyme shows reduced turnover rates and increased Km-value Escherichia coli
D369N mutant enzyme shows reduced turnover rates and increased Km-value. The reaction mechanism of the mutant enzyme involves only 1 metal with the possible assistance of a His side chain Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0094
-
p-nitrophenyl phosphate wild type enzyme, in absence of a phosphate acceptor Escherichia coli
0.02124
-
p-nitrophenyl phosphate wild type enzyme, in presence of a phosphate acceptor Escherichia coli
0.05972
-
p-nitrophenyl phosphate mutant enzyme D369N, in presence of a phosphate acceptor Escherichia coli
0.176
-
p-nitrophenyl phosphate mutant enzyme D369N, in absence of a phosphate acceptor Escherichia coli
2.941
-
p-nitrophenyl phosphate mutant enzyme D369A, in absence of a phosphate acceptor Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.01
-
p-nitrophenyl phosphate mutant enzyme D369A, in absence of a phosphate acceptor Escherichia coli
0.4
-
p-nitrophenyl phosphate mutant enzyme D369N, in absence of a phosphate acceptor Escherichia coli
44.5
-
p-nitrophenyl phosphate wild type enzyme Escherichia coli
80.5
-
p-nitrophenyl phosphate wild type enzyme, in presence of a phosphate acceptor Escherichia coli
230
-
p-nitrophenyl phosphate mutant enzyme D369N, in presence of a phosphate acceptor Escherichia coli